If you don’t know what it looks like, how are you supposed to understand its mechanisms? Listen to this year’s Nobel Laureate in Chemistry Richard Henderson, who has developed cryo-electron microscopy and thereby made it possible to capture each corner of the cell in atomic detail. The lecture is 14 December, at 15:30.

– You should really take the opportunity to listen to Richard Henderson. It is spectacular that we with his development within cryo-electron microscopy has reached the point where we can look at single amino acids within the proteins, says Johanna Höög, researcher at the Department of Chemistry and Molecular Biology, University of Gothenburg.

It took 15 years and many trips to the world’s sharpest electron microscopes before Richard Henderson in 1990 could present a structure of the purple-coloured protein Bacteriorhodopsin at atomic resolution. His discovery was then taken further by Jacques Dubochet and Joachim Frank, with whom Richard Henderson shares this year’s Nobel Prize "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".

Salmonella’s injection needle

Biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life's molecular machinery. The development of cryo-electron microscopy both simplifies and improves the imaging of biomolecules. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life's chemistry and for the development of pharmaceuticals.

For example, it is easier than ever before to depict membrane proteins, which often function as targets for pharmaceuticals, and to capture Salmonella’s injection needle for attacking cells.